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    OSBPL1A oxysterol binding protein like 1A [ Homo sapiens (human) ]

    Gene ID: 114876, updated on 2-May-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Host Lipid Transport Protein ORP1 Is Necessary for Coxiella burnetii Growth and Vacuole Expansion in Macrophages.

    Host Lipid Transport Protein ORP1 Is Necessary for Coxiella burnetii Growth and Vacuole Expansion in Macrophages.
    Schuler B, Sladek M, Gilk SD., Free PMC Article

    06/30/2023
    ORP1L mediated PI(4)P signaling at ER-lysosome-mitochondrion three-way contact contributes to mitochondrial division.

    ORP1L mediated PI(4)P signaling at ER-lysosome-mitochondrion three-way contact contributes to mitochondrial division.
    Boutry M, Kim PK., Free PMC Article

    10/23/2021
    Oxysterol-binding protein-related protein 1 variants have opposing cholesterol transport activities from the endolysosomes.

    Oxysterol-binding protein-related protein 1 variants have opposing cholesterol transport activities from the endolysosomes.
    Zhao K, Foster J, Ridgway ND., Free PMC Article

    06/5/2021
    ORP1 is a unique sensor of lysosomal phosphatidylinosito-bisphosphates, and that PI(4,5)P2/PI(3,4)P2 allosterically regulates cholesterol transport by ORP1.

    Allosteric enhancement of ORP1-mediated cholesterol transport by PI(4,5)P(2)/PI(3,4)P(2).
    Dong J, Du X, Wang H, Wang J, Lu C, Chen X, Zhu Z, Luo Z, Yu L, Brown AJ, Yang H, Wu JW., Free PMC Article

    04/13/2019
    structural and biochemical investigation of the Rab7-ORP1L interaction

    A non-canonical GTPase interaction enables ORP1L-Rab7-RILP complex formation and late endosome positioning.
    Ma X, Liu K, Li J, Li H, Li J, Liu Y, Yang C, Liang H., Free PMC Article

    03/2/2019
    ORP1L, via its liganding by lipids and the formation of contacts between autophagic vacuoles and the endoplasmic reticulum, governs the last steps in autophagy that lead to the lysosomal degradation of cytosolic material.

    Cholesterol and ORP1L-mediated ER contact sites control autophagosome transport and fusion with the endocytic pathway.
    Wijdeven RH, Janssen H, Nahidiazar L, Janssen L, Jalink K, Berlin I, Neefjes J., Free PMC Article

    09/1/2018
    This study validated that rs3746444 polymorphism influenced the expression of miR499a, its target gene, osbpl1a, and thereby associated with the HDL level, which makes it a potential factor involved in the mechanism of atherosclerosis.

    A single nucleotide polymorphism located in microRNA-499a causes loss of function resulting in increased expression of osbpl1a and reduced serum HDL level.
    Chen LB, Zheng HK, Zhang L, An Z, Wang XP, Shan RT, Zhang WQ.

    07/21/2018
    ORP1L-dependent membrane contacts between late endosomes/lysosomes and the endoplasmic reticulum coordinate cholesterol transfer with the retrograde movement of endo-lysosomal vesicles.

    Oxysterol-Binding Protein-Related Protein 1L Regulates Cholesterol Egress from the Endo-Lysosomal System.
    Zhao K, Ridgway ND.

    03/10/2018
    a familial loss-of-function mutation in OSBPL1A affects the first step of the reverse cholesterol transport process and associates with a low HDL-C phenotype

    A loss-of-function variant in OSBPL1A predisposes to low plasma HDL cholesterol levels and impaired cholesterol efflux capacity.
    Motazacker MM, Pirhonen J, van Capelleveen JC, Weber-Boyvat M, Kuivenhoven JA, Shah S, Hovingh GK, Metso J, Li S, Ikonen E, Jauhiainen M, Dallinga-Thie GM, Olkkonen VM.

    11/26/2017
    These data suggest that ORP1L is specifically recruited by the bacteria to the Coxiella parasitophorous vacuole, where it influences parasitophorous vacuole membrane dynamics and interactions with the endoplasmic reticulum.

    Interactions between the Coxiella burnetii parasitophorous vacuole and the endoplasmic reticulum involve the host protein ORP1L.
    Justis AV, Hansen B, Beare PA, King KB, Heinzen RA, Gilk SD., Free PMC Article

    08/5/2017
    ORP1L-VAP complexes also support transport of LDL-derived cholesterol from endosomes to the endoplasmic reticulum when ORP1L was bound to human adenovirus RIDalpha. RIDalpha-induced lipid trafficking also attenuated proinflammatory signaling by Toll-like receptor 4, which has a central role in adenovirus pathogenesis and is known to be tightly regulated by cholesterol-rich "lipid rafts."

    Adenovirus Modulates Toll-Like Receptor 4 Signaling by Reprogramming ORP1L-VAP Protein Contacts for Cholesterol Transport from Endosomes to the Endoplasmic Reticulum.
    Cianciola NL, Chung S, Manor D, Carlin CR., Free PMC Article

    05/20/2017
    Data suggest RIDalpha as a model system for understanding physiological egress routes that use ORP1L to activate endosome-to-endoplasmic reticulum (ER) feedback responses involved in lipid droplets (LDs)formation.

    Adenovirus RIDα uncovers a novel pathway requiring ORP1L for lipid droplet formation independent of NPC1.
    Cianciola NL, Greene DJ, Morton RE, Carlin CR., Free PMC Article

    07/5/2014
    ORP1S is a cytoplasmic sterol sensor, which transports sterols to the nucleus and promotes LXR regulated trans-activation of apoE.

    Sterol-dependent nuclear import of ORP1S promotes LXR regulated trans-activation of apoE.
    Lee S, Wang PY, Jeong Y, Mangelsdorf DJ, Anderson RG, Michaely P., Free PMC Article

    10/13/2012
    The study shows that OSBPL1A binds several oxysterols and cholesterol, and characterize a mutant, OSBPL1A Delta560-563, defective in oxysterol binding.

    Sterol binding by OSBP-related protein 1L regulates late endosome motility and function.
    Vihervaara T, Uronen RL, Wohlfahrt G, Björkhem I, Ikonen E, Olkkonen VM., Free PMC Article

    03/19/2011
    Observational study and genome-wide association study of gene-disease association. (HuGE Navigator)

    An integration of genome-wide association study and gene expression profiling to prioritize the discovery of novel susceptibility Loci for osteoporosis-related traits.
    Hsu YH, Zillikens MC, Wilson SG, Farber CR, Demissie S, Soranzo N, Bianchi EN, Grundberg E, Liang L, Richards JB, Estrada K, Zhou Y, van Nas A, Moffatt MF, Zhai G, Hofman A, van Meurs JB, Pols HA, Price RI, Nilsson O, Pastinen T, Cupples LA, Lusis AJ, Schadt EE, Ferrari S, Uitterlinden AG, Rivadeneira F, Spector TD, Karasik D, Kiel DP., Free PMC Article

    06/30/2010
    Clinical trial of gene-disease association and gene-environment interaction. (HuGE Navigator)

    Personalized smoking cessation: interactions between nicotine dose, dependence and quit-success genotype score.
    Rose JE, Behm FM, Drgon T, Johnson C, Uhl GR., Free PMC Article

    06/30/2010
    Results describe how ORP1L contacts VAP to control Rab7-RILP-p150 Glued and late endosome positioning.

    Cholesterol sensor ORP1L contacts the ER protein VAP to control Rab7-RILP-p150 Glued and late endosome positioning.
    Rocha N, Kuijl C, van der Kant R, Janssen L, Houben D, Janssen H, Zwart W, Neefjes J., Free PMC Article

    01/21/2010
    OSBPL1A was preferentially expressed from the maternal allele

    SNP-specific array-based allele-specific expression analysis.
    Bjornsson HT, Albert TJ, Ladd-Acosta CM, Green RD, Rongione MA, Middle CM, Irizarry RA, Broman KW, Feinberg AP., Free PMC Article

    01/21/2010
    binds to Rab7, modifies its functional cycle, and can interfere with lysosome organization and endocytic membrane trafficking.

    The oxysterol-binding protein homologue ORP1L interacts with Rab7 and alters functional properties of late endocytic compartments.
    Johansson M, Lehto M, Tanhuanpää K, Cover TL, Olkkonen VM., Free PMC Article

    01/21/2010
    Results suggest that the two forms of oxysterol binding protein-related protein-1 (ORP1) are functionally distinct and that ORP1L is involved in control of cellular lipid metabolism

    The two variants of oxysterol binding protein-related protein-1 display different tissue expression patterns, have different intracellular localization, and are functionally distinct.
    Johansson M, Bocher V, Lehto M, Chinetti G, Kuismanen E, Ehnholm C, Staels B, Olkkonen VM., Free PMC Article

    01/21/2010
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